3212-75-7Relevant articles and documents
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Loozen,H.J.J. et al.
, p. 418 - 422 (1977)
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Reese,Shaw
, p. 2566 (1970)
Synthesis, structure, magnetic and catalytic competency of a tetradentate (nnoo) schiff base mediated dimeric copper(ii) complex
CHOWDHURY, HABIBAR,BERA, RAJESH,ADHIKARY, CHANDAN
, p. 1280 - 1286 (2021/06/09)
One dinuclear copper(II) complex {μ-[2,2 -{ethane-1,2-diylbis[(azanylylidene)methanylylidene]}bis(phenolato)]}-{μ-[2,2 -{ethane-1,2- diylbis[(azanylylidene)methanylylidene]}bis(phenolato)]}dicopper(II), [Cu2(salen)2] (1) [salen2- = [2,2 -{ethane-1,2-diylbis- [(azanylylidene)methanylylidene]}bis(phenolato)] has been isolated and characterized by X-ray diffraction analysis and spectroscopic studies. X-ray single crystal structure examination revealed that each Cu(II) center in the asymmetric unit of 1 adopts a distorted square planar geometry with a CuN2O2 chromophore, where two asymmetric units are attached through congregation of Salen involving Cu-O bond to form dinuclear molecular unit [Cu2(salen)2]. In crystalline state, these dinuclear entities in 1 are extended through C-H π interactions and π π interactions displaying a 3D network structure. The variable-temperature magnetic susceptibility measurement asserted a dominant antiferromagnetic interaction between the copper(II) centers through Cu-O-Cu linkage in 1 with J = -1.46 cm-1. The catalytic efficacy of complex 1 was studied in a series of solvents for the oxidation of styrene and cyclooctene using tert-butyl-hydroperoxide (TBHP) as an active oxidant under mild conditions. The catalytic reaction mixture has been analyzed by gas chromatography and it displayed that the yield of the epoxidation and its selectivity is optimum in acetonitrile medium.
A Bioorthogonal Click Chemistry Toolbox for Targeted Synthesis of Branched and Well-Defined Protein–Protein Conjugates
Baalmann, Mathis,Bitsch, Sebastian,Deweid, Lukas,Ilkenhans, Nadja,Kolmar, Harald,Neises, Laura,Schneider, Hendrik,Werther, Philipp,Wilhelm, Jonas,Wolfring, Martin,Wombacher, Richard,Ziegler, Michael J.
supporting information, p. 12885 - 12893 (2020/06/02)
Bioorthogonal chemistry holds great potential to generate difficult-to-access protein–protein conjugate architectures. Current applications are hampered by challenging protein expression systems, slow conjugation chemistry, use of undesirable catalysts, or often do not result in quantitative product formation. Here we present a highly efficient technology for protein functionalization with commonly used bioorthogonal motifs for Diels–Alder cycloaddition with inverse electron demand (DAinv). With the aim of precisely generating branched protein chimeras, we systematically assessed the reactivity, stability and side product formation of various bioorthogonal chemistries directly at the protein level. We demonstrate the efficiency and versatility of our conjugation platform using different functional proteins and the therapeutic antibody trastuzumab. This technology enables fast and routine access to tailored and hitherto inaccessible protein chimeras useful for a variety of scientific disciplines. We expect our work to substantially enhance antibody applications such as immunodetection and protein toxin-based targeted cancer therapies.
